Q13478 · IL18R_HUMAN
- ProteinInterleukin-18 receptor 1
- GeneIL18R1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids541 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Within the IL18 receptor complex, responsible for the binding of the pro-inflammatory cytokine IL18, but not IL1A nor IL1B (PubMed:14528293, PubMed:25261253, PubMed:25500532, PubMed:37993714, PubMed:8626725).
Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850).
Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (By similarity).
Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850).
Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (By similarity).
Catalytic activity
- H2O + NAD+ = ADP-D-ribose + H+ + nicotinamideThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 455 | |||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin-18 receptor 1
- EC number
- Short namesIL-18R-1; IL-18R1
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13478
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-329 | Extracellular | ||||
Sequence: CTSRPHITVVEGEPFYLKHCSCSLAHEIETTTKSWYKSSGSQEHVELNPRSSSRIALHDCVLEFWPVELNDTGSYFFQMKNYTQKWKLNVIRRNKHSCFTERQVTSKIVEVKKFFQITCENSYYQTLVNSTSLYKNCKKLLLENNKNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVEDRSNIVPVLLGPKLNHVAVELGKNVRLNCSALLNEEDVIYWMFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVLYNCTVASTGGTDTKSFILVRKADMADIPGHVFTR | ||||||
Transmembrane | 330-350 | Helical | ||||
Sequence: GMIIAVLILVAVVCLVTVCVI | ||||||
Topological domain | 351-541 | Cytoplasmic | ||||
Sequence: YRVDLVLFYRHLTRRDETLTDGKTYDAFVSYLKECRPENGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNEVRYELESGLHEALVERKIKIILIEFTPVTDFTFLPQSLKLLKSHRVLKWKADKSLSYNSRFWKNLLYLMPAKTVKPGRDEPEVLPVLSES |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053379 | 210 | in dbSNP:rs11465635 | |||
Sequence: R → H | ||||||
Natural variant | VAR_053380 | 232 | in dbSNP:rs11465644 | |||
Sequence: N → K | ||||||
Mutagenesis | 297 | Decreases the affinity for IL18 suggesting that the N-linked glycosylation contributes to ligand recognition. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_053381 | 310 | in dbSNP:rs11465648 | |||
Sequence: S → N | ||||||
Natural variant | VAR_014955 | 317 | ||||
Sequence: Missing | ||||||
Natural variant | VAR_053382 | 423 | in dbSNP:rs12619169 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 699 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MNCRELPLTLWVLISVST | ||||||
Chain | PRO_0000015448 | 19-541 | Interleukin-18 receptor 1 | |||
Sequence: AESCTSRPHITVVEGEPFYLKHCSCSLAHEIETTTKSWYKSSGSQEHVELNPRSSSRIALHDCVLEFWPVELNDTGSYFFQMKNYTQKWKLNVIRRNKHSCFTERQVTSKIVEVKKFFQITCENSYYQTLVNSTSLYKNCKKLLLENNKNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVEDRSNIVPVLLGPKLNHVAVELGKNVRLNCSALLNEEDVIYWMFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVLYNCTVASTGGTDTKSFILVRKADMADIPGHVFTRGMIIAVLILVAVVCLVTVCVIYRVDLVLFYRHLTRRDETLTDGKTYDAFVSYLKECRPENGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNEVRYELESGLHEALVERKIKIILIEFTPVTDFTFLPQSLKLLKSHRVLKWKADKSLSYNSRFWKNLLYLMPAKTVKPGRDEPEVLPVLSES | ||||||
Disulfide bond | 22↔41 | |||||
Sequence: CTSRPHITVVEGEPFYLKHC | ||||||
Disulfide bond | 43↔81 | |||||
Sequence: CSLAHEIETTTKSWYKSSGSQEHVELNPRSSSRIALHDC | ||||||
Glycosylation | 91 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 102 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 119↔158 | |||||
Sequence: CFTERQVTSKIVEVKKFFQITCENSYYQTLVNSTSLYKNC | ||||||
Disulfide bond | 140↔185 | |||||
Sequence: CENSYYQTLVNSTSLYKNCKKLLLENNKNPTIKKNAEFEDQGYYSC | ||||||
Glycosylation | 150 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 236 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 237↔298 | |||||
Sequence: CSALLNEEDVIYWMFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVLYNC | ||||||
Glycosylation | 255 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated. N-linked glycosyl chains contribute to ligand recognition and intra-receptor interactions required for formation of an active ternary receptor complex.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in leukocytes, spleen, lung. Also expressed, but at lower levels, in liver, small intestine, colon, prostate, thymus, placenta, and heart. Specifically coexpressed with IL18R1 in Th1 cells (PubMed:10653850, PubMed:10925275, PubMed:11046021).
Induction
Induced by IL12/interleukin-12 in T-cells. Proposed to be a phenotypic marker for T-helper 1 (Th1) cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms a ternary complex with IL18 and IL18RAP (PubMed:14528293, PubMed:25500532).
Within this complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling leading to NF-kappa-B and JNK activation (Probable). Interacts with SLC12A3 in peritoneal macrophages; this interaction is increased by IL18 treatment (By similarity).
Within this complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling leading to NF-kappa-B and JNK activation (Probable). Interacts with SLC12A3 in peritoneal macrophages; this interaction is increased by IL18 treatment (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13478 | IL18 Q14116 | 2 | EBI-9817499, EBI-3910835 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-121 | Ig-like C2-type 1 | ||||
Sequence: GEPFYLKHCSCSLAHEIETTTKSWYKSSGSQEHVELNPRSSSRIALHDCVLEFWPVELNDTGSYFFQMKNYTQKWKLNVIRRNKHSCFT | ||||||
Domain | 133-212 | Ig-like C2-type 2 | ||||
Sequence: KKFFQITCENSYYQTLVNSTSLYKNCKKLLLENNKNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVEDRSN | ||||||
Domain | 220-312 | Ig-like C2-type 3 | ||||
Sequence: PKLNHVAVELGKNVRLNCSALLNEEDVIYWMFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVLYNCTVASTGGTDTKSFI | ||||||
Domain | 373-520 | TIR | ||||
Sequence: KTYDAFVSYLKECRPENGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNEVRYELESGLHEALVERKIKIILIEFTPVTDFTFLPQSLKLLKSHRVLKWKADKSLSYNSRFWKNLLYLM |
Domain
The TIR domain mediates NAD+ hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Sequence similarities
Belongs to the interleukin-1 receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length541
- Mass (Da)62,304
- Last updated1996-11-01 v1
- Checksum7173DB9C7EA71D32
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q86YL8 | Q86YL8_HUMAN | IL18R1 | 170 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U43672 EMBL· GenBank· DDBJ | AAC50390.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313967 EMBL· GenBank· DDBJ | BAG36682.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007248 EMBL· GenBank· DDBJ | AAY15048.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC069575 EMBL· GenBank· DDBJ | AAH69575.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093975 EMBL· GenBank· DDBJ | AAH93975.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093977 EMBL· GenBank· DDBJ | AAH93977.1 EMBL· GenBank· DDBJ | mRNA |